GroES binding regulates GroEL chaperonin activity under heat shock (Q73374291)

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3 November 2019

title

GroES binding regulates GroEL chaperonin activity under heat shock (English)

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3 November 2019

author name string

P Goloubinoff

1

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3 November 2019

S Diamant

2

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3 November 2019

C Weiss

3

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3 November 2019

A Azem

4

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3 November 2019

publication date

1 April 1997

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3 November 2019

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3 November 2019

volume

407

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3 November 2019

issue

2

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3 November 2019

page(s)

215-219

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The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

3 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

GroE facilitates refolding of citrate synthase by suppressing aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Biochemical Characterization of Symmetric GroEL-GroES Complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Increased efficiency of GroE-assisted protein folding by manganese ions

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Effect of divalent cations on the molecular structure of the GroEL oligomer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Homologous proteins with different affinities for groEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Protein folding in the cell: competing models of chaperonin function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2900348-7

10.1016/S0014-5793(97)00348-7

7 January 2021

Identifiers

DOI

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3 November 2019

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